ID   PSMF1_BOVIN             Reviewed;         270 AA.
AC   Q3SX30; Q1JPI8;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Proteasome inhibitor PI31 subunit;
GN   Name=PSMF1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays an important role in control of proteasome function.
CC       Inhibits the hydrolysis of protein and peptide substrates by the 20S
CC       proteasome. Also inhibits the activation of the proteasome by the
CC       proteasome regulatory proteins PA700 and PA28 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Monomer and homodimer. Interacts with FBXO7 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endoplasmic reticulum
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the proteasome inhibitor PI31 family.
CC       {ECO:0000305}.
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DR   EMBL; BT025365; ABF57321.1; -; mRNA.
DR   EMBL; BC104535; AAI04536.1; -; mRNA.
DR   RefSeq; NP_001069946.1; NM_001076478.1.
DR   AlphaFoldDB; Q3SX30; -.
DR   SMR; Q3SX30; -.
DR   STRING; 9913.ENSBTAP00000024505; -.
DR   PaxDb; Q3SX30; -.
DR   PRIDE; Q3SX30; -.
DR   Ensembl; ENSBTAT00000024505; ENSBTAP00000024505; ENSBTAG00000018417.
DR   GeneID; 617807; -.
DR   KEGG; bta:617807; -.
DR   CTD; 9491; -.
DR   VEuPathDB; HostDB:ENSBTAG00000018417; -.
DR   VGNC; VGNC:33477; PSMF1.
DR   eggNOG; KOG4761; Eukaryota.
DR   GeneTree; ENSGT00390000012257; -.
DR   HOGENOM; CLU_090116_0_0_1; -.
DR   InParanoid; Q3SX30; -.
DR   OMA; NICVEPE; -.
DR   OrthoDB; 1614691at2759; -.
DR   TreeFam; TF106238; -.
DR   Proteomes; UP000009136; Chromosome 13.
DR   Bgee; ENSBTAG00000018417; Expressed in choroid plexus and 108 other tissues.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR   GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR   GO; GO:0070628; F:proteasome binding; ISS:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:1901799; P:negative regulation of proteasomal protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   InterPro; IPR045128; PI31-like.
DR   InterPro; IPR013886; PI31_Prot_C.
DR   InterPro; IPR021625; PI31_Prot_N.
DR   PANTHER; PTHR13266; PTHR13266; 1.
DR   Pfam; PF08577; PI31_Prot_C; 1.
DR   Pfam; PF11566; PI31_Prot_N; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Endoplasmic reticulum; Methylation; Phosphoprotein;
KW   Proteasome; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q92530"
FT   CHAIN           2..270
FT                   /note="Proteasome inhibitor PI31 subunit"
FT                   /id="PRO_0000261313"
FT   REGION          2..150
FT                   /note="Important for homodimerization and interaction with
FT                   FBXO7"
FT                   /evidence="ECO:0000250"
FT   REGION          220..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92530"
FT   MOD_RES         152
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92530"
FT   MOD_RES         204
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BHL8"
FT   MOD_RES         218
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BHL8"
FT   MOD_RES         230
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92530"
FT   MOD_RES         251
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92530"
FT   CONFLICT        203
FT                   /note="R -> W (in Ref. 2; AAI04536)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   270 AA;  29705 MW;  5131EDCB033ED71E CRC64;
     MAGLEVLFAS AAPAITCAQD ALVCFLHWEV VTHGYYGLGA GDQPGPNDKK SELLPVEWNS
     NKDLYVLRYE SKDGSRKLLV KAVTVENSMI INVLEHGSQQ VSDLTLNLND YIDSEHLVDF
     HRVYKNSEEL RSRIVSGIIT PIHEQWEKAN LSPHREFPPA TAREVDPLRI HPQHPHTSRQ
     PTWCDPLGPF AVGGEDLDPF GCRRGGMIVD PLRSGFPRAL IDPSSGLPNR LPPGAVPPGA
     RFDPFGPIGT SPSGPNPDHL PPPGYDDMYL